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3KEK

Crystal Structure of Human MMP-13 complexed with a (pyridin-4-yl)-2H-tetrazole compound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004222molecular_functionmetalloendopeptidase activity
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0031012cellular_componentextracellular matrix
B0004222molecular_functionmetalloendopeptidase activity
B0006508biological_processproteolysis
B0008237molecular_functionmetallopeptidase activity
B0008270molecular_functionzinc ion binding
B0031012cellular_componentextracellular matrix
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 901
ChainResidue
AHIS222
AHIS226
AHIS232
AHOH2040
AHOH2159

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 902
ChainResidue
AHIS172
AASP174
AHIS187
AHIS200

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 903
ChainResidue
AASP179
AGLY180
ASER182
ALEU184
AASP202
AGLU205

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 904
ChainResidue
AALA161
AASP162
AASN194
AGLY196
AASP198
AHOH2007
AHOH2266

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 905
ChainResidue
AASP128
AASP203
AGLU205

site_idAC6
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 3EK A 801
ChainResidue
ALYS140
AASN215
APHE217
ALEU218
AVAL219
AHIS222
AALA238
ALEU239
APHE241
AILE243
ATYR244
ATHR245
ATYR246
ATHR247
ALYS249
ASER250
APRO255
AHOH2039
AHOH2062
AHOH2065
AHOH2094
AHOH2146
AHOH2208

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 901
ChainResidue
BHIS222
BHIS226
BHIS232
BHOH2079
BHOH2130

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 902
ChainResidue
BHIS172
BASP174
BHIS187
BHIS200

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 903
ChainResidue
BASP179
BGLY180
BSER182
BLEU184
BASP202
BGLU205

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 904
ChainResidue
BALA161
BASP162
BASN194
BGLY196
BASP198

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA B 905
ChainResidue
BASP128
BGLU205
BTHR206
BHOH2254

site_idBC3
Number of Residues23
DetailsBINDING SITE FOR RESIDUE 3EK B 801
ChainResidue
BLYS140
BASN215
BPHE217
BLEU218
BVAL219
BHIS222
BALA238
BLEU239
BPHE241
BPRO242
BILE243
BTYR244
BTHR245
BTYR246
BTHR247
BLYS249
BSER250
BPRO255
BHOH2008
BHOH2101
BHOH2149
BHOH2166
BHOH2244

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VAAHEFGHSL
ChainResidueDetails
AVAL219-LEU228

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:23913860
ChainResidueDetails
AHIS222
BHIS222

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860, ECO:0000269|PubMed:8969305
ChainResidueDetails
APRO127
APHE201
AASP202
AASP204
BPRO127
BALA161
BPHE178
BASP179
BPRO181
BGLY183
BPRO193
AALA161
BTYR195
BGLY197
BPHE201
BASP202
BASP204
APHE178
AASP179
APRO181
AGLY183
APRO193
ATYR195
AGLY197

site_idSWS_FT_FI3
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:10926524, ECO:0000269|PubMed:10986126, ECO:0000269|PubMed:15734645, ECO:0000269|PubMed:15780611, ECO:0000269|PubMed:17196980, ECO:0000269|PubMed:17623656, ECO:0000269|PubMed:19422229, ECO:0000269|PubMed:20005097, ECO:0000269|PubMed:20726512, ECO:0000269|PubMed:22689580, ECO:0000269|PubMed:23810497, ECO:0000269|PubMed:23913860
ChainResidueDetails
AGLU171
BGLY173
BALA186
BALA199
BALA221
BGLY225
BASP231
BLEU239
AGLY173
AALA186
AALA199
AALA221
AGLY225
AASP231
ALEU239
BGLU171

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8576151
ChainResidueDetails
AMET116
BMET116

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
ALEU151
BLEU151

218853

PDB entries from 2024-04-24

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